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Title:
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins - PubMed
Description:
The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was recently discovered in mammalian tissues and purified from porcine kidney. It catalyses the slow cis-trans isomerization of proline peptide (Xaa-Pro) bonds in oligopeptides and accelerates slow, rate-limiting steps in the folding of several …
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Keywords {🔍}
pmid, doi, isomerase, cyclophilin, protein, peptidylprolyl, nature, cistrans, pmc, proteins, ppiase, folding, sequence, free, article, metabolism, abstract, articles, cited, mesh, oligopeptides, cyclosporin, csa, molecular, prolyl, acid, main, ncbi, similar, related, resources, identical, schmid, proline, catalysis, pubmed, aug, review, amino, hhs, page, content, homepage, navigation, search, full, text, comment, publication, types,
Topics {✒️}
38 amino-acid residues n-terminal sequence relative molecular mass peptidyl-prolyl cis-trans isomerase peptidyl-prolyl cis-trans-isomerase nucleic acid spectrometry sequence porcine kidney o-acylation-directed lead optimization similar articles cited main page content proline peptide mesh keyword slow cis-trans isomerization oligopeptides prolyl isomerase activity catalysis 1696687 catalysis fk506-binding protein identical proteins prolyl isomerase proteins catalyses protein folding isomerase modification single sulphydryl group protein folding united states government rate-limiting steps related cypa inhibitory mechanism n-terminal sequencing distinct mitochondrial cyclophilin literature sources prolyl isomerization 1038/337476a0 abstract cited recently discovered mammalian tissues accelerates slow abstract hhs schmid fx linkout pubmed wordmark pubmed logo official website wittmann-liebold xaa-pro enzymatic properties binds tightly
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